Reviewed, UniProtKB/Swiss-Prot O48646 (GPX6_ARATH)

Names and origin

Protein names

Recommended name:
    Probable phospholipid hydroperoxide glutathione peroxidase 6, mitochondrial
      Short name=PHGPx
      Short name=AtGPX1
    EC=1.11.1.12

Gene names

Name:	GPX6
Synonyms:	GPX1
Ordered Locus Names:	At4g11600
ORF Names:	T5C23.30

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	232 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione By similarity.
Catalytic activity	2 glutathione + a lipid hydroperoxide = glutathione disulfide + lipid + 2 H(2)O.
Subcellular location	MitochondrionPotential.
Tissue specificity	Expressed at a low but detectable level in leaves, stems, and flowers, but at a higher level in siliques and even higher in roots. Predominantly expressed in seeds.
Induction	By salt stress, osmotic stress, cold treatment, and metals. Up-regulated by salicylic acid (SA), jasmonic acid (JA), abscisic acid (ABA) and auxin.
Sequence similarities	Belongs to the glutathione peroxidase family.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Mitochondrion
Domain	Transit peptide
Molecular function	Oxidoreductase Peroxidase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to oxidative stress Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	glutathione peroxidase activity Inferred from electronic annotation. Source: InterPro phospholipid-hydroperoxide glutathione peroxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 54	54	Mitochondrion Potential
	Chain	55 – 232	178	Probable phospholipid hydroperoxide glutathione peroxidase 6, mitochondrial		PRO_0000013088
Sites
	Active site	105	1	By similarity
Experimental info
	Sequence conflict	30	1	S → SSSS Ref.1
	Sequence conflict	51	1	S → Y Ref.5

Sequences

	Sequence		Length	Mass (Da)
	O48646-1 [UniParc]. Last modified May 10, 2004. Version 2. Checksum: 93F3084A8A331494	FASTA	232	25,584
	10 20 30 40 50 60 MLRSSIRLLY IRRTSPLLRS LSSSSSSSSS KRFDSAKPLF NSHRIISLPI STTGAKLSRS 70 80 90 100 110 120 EHSMAASSEP KSLYDFTVKD AKGNDVDLSI YKGKVLLIVN VASQCGLTNS NYTELAQLYE 130 140 150 160 170 180 KYKGHGFEIL AFPCNQFGNQ EPGTNEEIVQ FACTRFKAEY PIFDKVDVNG DKAAPVYKFL 190 200 210 220 230 KSSKGGLFGD GIKWNFAKFL VDKDGNVVDR FAPTTSPLSI EKDVKKLLGV TA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of a cDNA encoding a putative glutathione peroxidase protein from Arabidopsis thaliana." Bilodeau P., Luo M., Dennis E.S., Peacock W.J., Chaudhury A.M. (er) Plant Gene Register PGR98-047 Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION. Strain: cv. Landsberg erecta.
[2]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-232.
[5]	"Putative phospholipid hydroperoxide glutathione peroxidase gene from Arabidopsis thaliana induced by oxidative stress." Sugimoto M., Sakamoto W. Genes Genet. Syst. 72:311-316(1997) [PubMed: 9511228] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 31-232, INDUCTION. Strain: cv. Columbia.
[6]	"Glutathione peroxidase genes in Arabidopsis are ubiquitous and regulated by abiotic stresses through diverse signaling pathways." Rodriguez Milla M.A., Maurer A., Rodriguez Huete A., Gustafson J.P. Plant J. 36:602-615(2003) [PubMed: 14617062] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, INDUCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF030132 mRNA. Translation: AAC09173.1. Different initiation. AL049500 Genomic DNA. Translation: CAB39931.1. Different initiation. AL161532 Genomic DNA. Translation: CAB78203.1. Different initiation. AY039863 mRNA. Translation: AAK63967.1. AY077655 mRNA. Translation: AAL76133.1. AY088647 mRNA. Translation: AAM66969.1. Different initiation. AB001568 mRNA. Translation: BAA24226.1. Different initiation.
PIR	T04207.
RefSeq	NP_192897.2.
UniGene	At.23184
3D structure databases
HSSP	HSSP built from PDB template 1GP1 based on UniProtKB P00435.
ModBase	Search...
Protein family/group databases
PeroxiBase	2502. AtGPx06.
Genome annotation databases
GeneID	826765.
GenomeReviews	Gene locus AT4G11600 in contig CT486007_GR.
KEGG	ath:AT4G11600.
NMPDR	fig|3702.1.peg.18828.
Organism-specific databases
GeneFarm	2055. 163.
TAIR	At4g11600.
Gene expression databases
ArrayExpress	O48646.
GermOnline	AT4G11600. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR000889. Glut_peroxidase. IPR001452. SH3. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PANTHER	PTHR11592. Glut_peroxidase. 1 hit.
Pfam	PF00255. GSHPx. 1 hit. [Graphical view]
PIRSF	PIRSF000303. Glutathion_perox. 1 hit.
PRINTS	PR01011. GLUTPROXDASE. PR00452. SH3DOMAIN.
PROSITE	PS00460. GLUTATHIONE_PEROXID_1. 1 hit. PS00763. GLUTATHIONE_PEROXID_2. 1 hit. PS51355. GLUTATHIONE_PEROXID_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GPX6_ARATH

Accession

Primary (citable) accession number: O48646
Secondary accession number(s): Q94BV3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 27, 2002
Last sequence update:	May 10, 2004
Last modified:	November 25, 2008
This is version 64 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)